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Volumn 75, Issue 4-5, 2010, Pages 330-337

Probing the binding pocket of the active site of aromatase with 2-phenylaliphatic androsta-1,4-diene-3,17-dione steroids

Author keywords

2 Phenylaliphatic substituent; Androsta 1,4 diene 3,17 dione; Aromatase; Breast cancer; Competitive inhibitor; Suicide substrate

Indexed keywords

2 BENZYL ANDROSTA 1,4 DIENE 3,17 DIONE; 2 PENTO METHYLPHENETHYL ANDROSTA 1,4 DIENE 3,17 DIONE; 2 PENTO TRIFLUOROMETHYLPHENETHYL ANDROSTA 1,4 DIENE 3,17 DIONE; 2 PHENBUTYL ANDROSTA 1,4 DIENE 3,17 DIONE; 2 PHENETHYL ANDROSTA 1,4 DIENE 3,17 DIONE; 2 PHENPROPYL ANDROSTA 1,4 DIENE 3,17 DIONE; 2ALPHA BENZYL ANDROSTENEDIONE; 2ALPHA PENTO METHYLPHENETHYL ANDROSTENEDIONE; 2ALPHA PENTO TRIFLUOROMETHYLPHENETHYL ANDROSTENEDIONE; 2ALPHA PHENBUTYL ANDROSTENEDIONE; 2ALPHA PHENETHYL ANDROSTENEDIONE; 2ALPHA PHENPROPYL ANDROSTENEDIONE; ANDROSTENEDIONE; ANDROSTENEDIONE DERIVATIVE; AROMATASE; AROMATASE INHIBITOR; CYSTEINE; UNCLASSIFIED DRUG;

EID: 77949264904     PISSN: 0039128X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.steroids.2010.01.008     Document Type: Article
Times cited : (11)

References (41)
  • 1
    • 0016272566 scopus 로고
    • The involvement of human placental microsomal cytochrome P-450 in aromatization
    • Thompson Jr. E.A., and Siiteri P.K. The involvement of human placental microsomal cytochrome P-450 in aromatization. J Biol Chem 249 (1974) 5373-5378
    • (1974) J Biol Chem , vol.249 , pp. 5373-5378
    • Thompson Jr., E.A.1    Siiteri, P.K.2
  • 2
    • 0023180688 scopus 로고
    • Purification and characterization of human placental aromatase cytochrome P-450
    • Kellis Jr. J., and Vickery L.E. Purification and characterization of human placental aromatase cytochrome P-450. J Biol Chem 262 (1987) 4413-4420
    • (1987) J Biol Chem , vol.262 , pp. 4413-4420
    • Kellis Jr., J.1    Vickery, L.E.2
  • 3
    • 0025872595 scopus 로고
    • Purification of human placental aromatase cytochrome P-450 with monoclonal antibody and its characterization
    • Yoshida N., and Osawa Y. Purification of human placental aromatase cytochrome P-450 with monoclonal antibody and its characterization. Biochemistry 30 (1991) 3003-3010
    • (1991) Biochemistry , vol.30 , pp. 3003-3010
    • Yoshida, N.1    Osawa, Y.2
  • 4
    • 0016293443 scopus 로고
    • Utilization of oxygen and reduced nicotinamide adenine dinucleotide phosphate by human placental microsomes during aromatization of androstenedione
    • Thompson Jr. E.A., and Siiteri P.K. Utilization of oxygen and reduced nicotinamide adenine dinucleotide phosphate by human placental microsomes during aromatization of androstenedione. J Biol Chem 249 (1974) 5364-5372
    • (1974) J Biol Chem , vol.249 , pp. 5364-5372
    • Thompson Jr., E.A.1    Siiteri, P.K.2
  • 5
    • 0001828104 scopus 로고
    • Aromatase inhibitors: specific inhibitors of estrogen biosynthesis
    • Berg D., and Plempel M. (Eds), Eliss Horwood Ltd., Chichester
    • Covey D.F. Aromatase inhibitors: specific inhibitors of estrogen biosynthesis. In: Berg D., and Plempel M. (Eds). Sterol biosynthesis inhibitors: pharmaceutical and agrochemical aspects (1988), Eliss Horwood Ltd., Chichester 534-571
    • (1988) Sterol biosynthesis inhibitors: pharmaceutical and agrochemical aspects , pp. 534-571
    • Covey, D.F.1
  • 6
    • 0027273894 scopus 로고
    • Mechanism of human placental aromatase: a new active site model
    • Oh S.S., and Robinson C.H. Mechanism of human placental aromatase: a new active site model. J Steroid Biochem Mol Biol 44 (1993) 389-397
    • (1993) J Steroid Biochem Mol Biol , vol.44 , pp. 389-397
    • Oh, S.S.1    Robinson, C.H.2
  • 8
    • 0027057856 scopus 로고
    • Inhibitors of P450-dependent steroid biosynthesis: from research to medical treatment
    • Bossche H.V. Inhibitors of P450-dependent steroid biosynthesis: from research to medical treatment. J Steroid Biochem Mol Biol 43 (1992) 1003-1021
    • (1992) J Steroid Biochem Mol Biol , vol.43 , pp. 1003-1021
    • Bossche, H.V.1
  • 9
    • 0028018928 scopus 로고
    • Aromatase and its inhibitors in breast cancer treatment-overview and perspective
    • Brodie A.M., and Santen R.J. Aromatase and its inhibitors in breast cancer treatment-overview and perspective. Breast Cancer Res Treat 30 (1994) 1-6
    • (1994) Breast Cancer Res Treat , vol.30 , pp. 1-6
    • Brodie, A.M.1    Santen, R.J.2
  • 11
    • 0034991842 scopus 로고    scopus 로고
    • Recent advances in the clinical application of aromatase inhibitors
    • Harper-Wynne C., and Dowsett M. Recent advances in the clinical application of aromatase inhibitors. J Steroid Biochem Mol Biol 76 (2001) 179-186
    • (2001) J Steroid Biochem Mol Biol , vol.76 , pp. 179-186
    • Harper-Wynne, C.1    Dowsett, M.2
  • 12
    • 0142216815 scopus 로고
    • Biological aromatization of steroids
    • Ryan K.J. Biological aromatization of steroids. J Biol Chem 234 (1959) 268-272
    • (1959) J Biol Chem , vol.234 , pp. 268-272
    • Ryan, K.J.1
  • 14
    • 0015216939 scopus 로고
    • Enzymatic aromatization of steroids. I. Effects of oxygen and carbon monoxide on the intermediate steps of estrogen biosynthesis
    • Meigs R.A., and Ryan K.J. Enzymatic aromatization of steroids. I. Effects of oxygen and carbon monoxide on the intermediate steps of estrogen biosynthesis. J Biol Chem 246 (1971) 83-87
    • (1971) J Biol Chem , vol.246 , pp. 83-87
    • Meigs, R.A.1    Ryan, K.J.2
  • 15
    • 0019780075 scopus 로고
    • Metabolism of 1,4-androstadiene-3,17-dione by human placental microsomes. Enzyme properties and kinetic parameters in the formation of estrogens and 17β-hydroxy-1,4-androstadien-3-one
    • Milewich L., Bradfield D.J., Coe L.D., Masters B.S.S., and MacDonald P. Metabolism of 1,4-androstadiene-3,17-dione by human placental microsomes. Enzyme properties and kinetic parameters in the formation of estrogens and 17β-hydroxy-1,4-androstadien-3-one. J Steroid Biochem 14 (1981) 1115-1125
    • (1981) J Steroid Biochem , vol.14 , pp. 1115-1125
    • Milewich, L.1    Bradfield, D.J.2    Coe, L.D.3    Masters, B.S.S.4    MacDonald, P.5
  • 16
    • 0031982998 scopus 로고    scopus 로고
    • Enzymic aromatization of 6-alkyl-substituted androgens, potent competitive and mechanism-based inhibitors of aromatase
    • Numazawa M., Yoshimura A., and Oshibe M. Enzymic aromatization of 6-alkyl-substituted androgens, potent competitive and mechanism-based inhibitors of aromatase. Biochem J 329 (1998) 151-156
    • (1998) Biochem J , vol.329 , pp. 151-156
    • Numazawa, M.1    Yoshimura, A.2    Oshibe, M.3
  • 17
    • 0032585724 scopus 로고    scopus 로고
    • 1,4,6- androgens and their 6-alkyl analogs, potent inhibitors of aromatase
    • 1,4,6- androgens and their 6-alkyl analogs, potent inhibitors of aromatase. J Steroid Biochem Mol Biol 70 (1999) 189-196
    • (1999) J Steroid Biochem Mol Biol , vol.70 , pp. 189-196
    • Numazawa, M.1    Yoshimura, A.2
  • 18
    • 0015594143 scopus 로고
    • Studies on the mechanism of estrogen biosynthesis. VIII. The development of inhibitors of the enzyme system in human placenta
    • Schwarzel W.C., Kruggel W.G., and Brodie H.J. Studies on the mechanism of estrogen biosynthesis. VIII. The development of inhibitors of the enzyme system in human placenta. Endocrinology 92 (1973) 866-880
    • (1973) Endocrinology , vol.92 , pp. 866-880
    • Schwarzel, W.C.1    Kruggel, W.G.2    Brodie, H.J.3
  • 19
    • 0019449456 scopus 로고
    • Enzyme-generated intermediates derived from 4-androstene-3,6,17-trione and 1,4,6-androstatriene-3,17-dione cause a time-dependent decrease in human placental aromatase activity
    • Covey D.F., and Hood W.F. Enzyme-generated intermediates derived from 4-androstene-3,6,17-trione and 1,4,6-androstatriene-3,17-dione cause a time-dependent decrease in human placental aromatase activity. Endocrinology 108 (1981) 1597-1599
    • (1981) Endocrinology , vol.108 , pp. 1597-1599
    • Covey, D.F.1    Hood, W.F.2
  • 20
    • 0019978673 scopus 로고
    • A new hypothesis based on suicide substrate inhibitor studies for the mechanism of action of aromatase
    • Covey D.F., and Hood W.F. A new hypothesis based on suicide substrate inhibitor studies for the mechanism of action of aromatase. Cancer Res 42 Suppl. (1982) 3327s-3333s
    • (1982) Cancer Res , vol.42 , Issue.SUPPL
    • Covey, D.F.1    Hood, W.F.2
  • 21
    • 0021848341 scopus 로고
    • Aromatase inhibitors. Synthesis and biological activity of androstenedione derivatives
    • Marsh D.A., Brodie H.J., Garrett W., Tsai-Morris C.H., and Brodie A.M.H. Aromatase inhibitors. Synthesis and biological activity of androstenedione derivatives. J Med Chem 28 (1985) 788-795
    • (1985) J Med Chem , vol.28 , pp. 788-795
    • Marsh, D.A.1    Brodie, H.J.2    Garrett, W.3    Tsai-Morris, C.H.4    Brodie, A.M.H.5
  • 23
    • 7844221897 scopus 로고
    • 1-Testololactone, a nonadrogenic augmentor and inhibitor of androgens
    • 1-Testololactone, a nonadrogenic augmentor and inhibitor of androgens. Cancer 13 (1960) 1201-1205
    • (1960) Cancer , vol.13 , pp. 1201-1205
    • Lerner, L.J.1    Bianchi, A.2    Borman, A.3
  • 24
    • 0022550064 scopus 로고
    • 1-Methyl-1,4-androstadiene-3,17-dione (SH 489): characterization of an irreversible inhibitor of estrogen biosynthesis
    • Henderson D., Norbisrath G., and Kerb U. 1-Methyl-1,4-androstadiene-3,17-dione (SH 489): characterization of an irreversible inhibitor of estrogen biosynthesis. J Steroid Biochem 24 (1986) 303-306
    • (1986) J Steroid Biochem , vol.24 , pp. 303-306
    • Henderson, D.1    Norbisrath, G.2    Kerb, U.3
  • 25
    • 0024817037 scopus 로고
    • Aromatase inhibition and experimental antitumor activity of FCE 24304, MDL 18962 and SH 489
    • Salle E.D., Briatico G., Giudici D., Ornati G., and Zaccheo T. Aromatase inhibition and experimental antitumor activity of FCE 24304, MDL 18962 and SH 489. J Steroid Biochem 34 (1989) 431-434
    • (1989) J Steroid Biochem , vol.34 , pp. 431-434
    • Salle, E.D.1    Briatico, G.2    Giudici, D.3    Ornati, G.4    Zaccheo, T.5
  • 27
    • 0029971786 scopus 로고    scopus 로고
    • Time-dependent inactivation of aromatase by 6-alkylandrosta-1,4-diene-3,17-diones. Effects of length and configuration of 6-alkyl group
    • Numazawa M., Oshibe M., Yamaguchi S., and Tachibana M. Time-dependent inactivation of aromatase by 6-alkylandrosta-1,4-diene-3,17-diones. Effects of length and configuration of 6-alkyl group. J Med Chem 39 (1996) 1033-1038
    • (1996) J Med Chem , vol.39 , pp. 1033-1038
    • Numazawa, M.1    Oshibe, M.2    Yamaguchi, S.3    Tachibana, M.4
  • 28
    • 0032979982 scopus 로고    scopus 로고
    • 19 steroids having a 1,4-diene, 4,6-diene, or 1,4,6-triene structure as aromatase inhibitors
    • 19 steroids having a 1,4-diene, 4,6-diene, or 1,4,6-triene structure as aromatase inhibitors. Steroids 64 (1999) 187-196
    • (1999) Steroids , vol.64 , pp. 187-196
    • Numazawa, M.1    Yamaguchi, S.2
  • 29
    • 0033758790 scopus 로고    scopus 로고
    • Probing the binding pocket of the active site of aromatase with 6-ether or 6-ester substituted androst-4-ene-3,17-diones and their diene and triene analogs
    • Numazawa M., Shelangouski M., and Nagasaka M. Probing the binding pocket of the active site of aromatase with 6-ether or 6-ester substituted androst-4-ene-3,17-diones and their diene and triene analogs. Steroids 65 (2000) 871-882
    • (2000) Steroids , vol.65 , pp. 871-882
    • Numazawa, M.1    Shelangouski, M.2    Nagasaka, M.3
  • 30
    • 34548502695 scopus 로고    scopus 로고
    • Studies directed towards a mechanistic evaluation of inactivation of aromatase by the suicide substrates androta-1,4-diene-3,17-diones and its 6-ene derivatives. Aromatase inactivation by the 19-substituted derivatives and their enzymic aromatization
    • Numazawa M., Nagaoka M., Handa W., Ogawa Y., and Matsuoka S. Studies directed towards a mechanistic evaluation of inactivation of aromatase by the suicide substrates androta-1,4-diene-3,17-diones and its 6-ene derivatives. Aromatase inactivation by the 19-substituted derivatives and their enzymic aromatization. J Steroid Biochem Mol Biol 107 (2007) 211-219
    • (2007) J Steroid Biochem Mol Biol , vol.107 , pp. 211-219
    • Numazawa, M.1    Nagaoka, M.2    Handa, W.3    Ogawa, Y.4    Matsuoka, S.5
  • 31
    • 67650659854 scopus 로고    scopus 로고
    • Aromatase inactivation by 2-substituted derivatives of the suicide substrate androsta-1,4-diene-3,17-dione
    • Takahashi M., Handa W., Umeta H., Ishikawa S., Yamashita K., and Numazawa M. Aromatase inactivation by 2-substituted derivatives of the suicide substrate androsta-1,4-diene-3,17-dione. J Steroid Biochem Mol Biol 116 (2009) 191-199
    • (2009) J Steroid Biochem Mol Biol , vol.116 , pp. 191-199
    • Takahashi, M.1    Handa, W.2    Umeta, H.3    Ishikawa, S.4    Yamashita, K.5    Numazawa, M.6
  • 33
    • 33746133501 scopus 로고
    • Addition of hydrogen chloride and iodide to olefins. Undecenoic acid
    • Abraham E.P., and Smith J.C. Addition of hydrogen chloride and iodide to olefins. Undecenoic acid. J Chem Soc (1936) 1605-1607
    • (1936) J Chem Soc , pp. 1605-1607
    • Abraham, E.P.1    Smith, J.C.2
  • 34
    • 0035815140 scopus 로고    scopus 로고
    • A novel route to the marasmane skeleton via a tandem rearrangement-cyclopropanation reaction. Total synthesis of (+)-isovelleral
    • Roel B., Joannes W., and Aede G. A novel route to the marasmane skeleton via a tandem rearrangement-cyclopropanation reaction. Total synthesis of (+)-isovelleral. J Org Chem 66 (2001) 2350-2357
    • (2001) J Org Chem , vol.66 , pp. 2350-2357
    • Roel, B.1    Joannes, W.2    Aede, G.3
  • 35
    • 0000392886 scopus 로고
    • The kinetically controlled methylation of conjugated polycyclic ketones
    • Nedelec L., Gasc J.C., and Bucourt R. The kinetically controlled methylation of conjugated polycyclic ketones. Tetrahedron 30 (1974) 3263-3268
    • (1974) Tetrahedron , vol.30 , pp. 3263-3268
    • Nedelec, L.1    Gasc, J.C.2    Bucourt, R.3
  • 37
    • 70349201570 scopus 로고    scopus 로고
    • Autodock Vina: improving the speed and accuracy of docking with a new scoring function, efficient optimization and multithreading
    • available online
    • Trott A., and Olson J. Autodock Vina: improving the speed and accuracy of docking with a new scoring function, efficient optimization and multithreading. J Comput Chem (2009) available online
    • (2009) J Comput Chem
    • Trott, A.1    Olson, J.2
  • 38
    • 73649151319 scopus 로고
    • Effects of methanesulfonic acid as irreversible inhibitors of acetylcholine esterase
    • Kitz R., and Wilson I.B. Effects of methanesulfonic acid as irreversible inhibitors of acetylcholine esterase. J Biol Chem 237 (1962) 3245-3249
    • (1962) J Biol Chem , vol.237 , pp. 3245-3249
    • Kitz, R.1    Wilson, I.B.2
  • 40
    • 58549095640 scopus 로고    scopus 로고
    • Chemical aromatization of 19-hydroxyandrosta-1,4-diene-3,17-dione with acid or alkaline: elimination of the 19-hydroxy methyl group as formaldehyde
    • Numazawa M., Yamashita K., Kimura N., and Takahashi M. Chemical aromatization of 19-hydroxyandrosta-1,4-diene-3,17-dione with acid or alkaline: elimination of the 19-hydroxy methyl group as formaldehyde. Steroids 74 (2009) 208-211
    • (2009) Steroids , vol.74 , pp. 208-211
    • Numazawa, M.1    Yamashita, K.2    Kimura, N.3    Takahashi, M.4
  • 41
    • 58149339806 scopus 로고    scopus 로고
    • Structural basis for androgen specificity and oestrogen synthesis in human aromatase
    • Ghosh D., Griswold J., Erman M., and Pangborn W. Structural basis for androgen specificity and oestrogen synthesis in human aromatase. Nature 457 (2009) 219-223
    • (2009) Nature , vol.457 , pp. 219-223
    • Ghosh, D.1    Griswold, J.2    Erman, M.3    Pangborn, W.4


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